Casein Kinase I (CK1)
- This product was discontinued on January 01, 2017
Casein Kinase I (CK1) is a serine/threonine protein kinase (1). It is a truncated monomer (1-317) of the CK1d isoform, which lacks the regulatory C-terminal domain, containing 111 amino acids (2). In vitro studies have shown that the activity of CK1δ is regulated by autophosphorylation of its C-terminal domain. Autophosphorylation of this domain on potential sites leads to inhibition of kinase activity (3). There are at least seven mammalian CK1 isoforms and their splice variants, and distinct CK1 family members have a variety of roles in eukaryotic cells (4).
- Protein serine/threonine kinase
- Rat, recombinant (E. coli)
Product SourceIsolated from a strain of E. coli that carries a clone expressing CK1 δ derived from a rat testis cDNA library (kindly provided by Dr. P. J. Roach). Two codons, Ser-318 and Arg-319, have been changed to stop codons, resulting in a truncation of the C-terminal portion of the expressed protein (2).
Recognition DeterminantThe most effective recognition motif for phosphorylation by CK1 is pSXXS/T where Ser in the position -3 is phosphorylated (3). Also, the clusters of 3 or 4 acidic residues ending at the position -3, preferably Asp, can specify phosphorylation by CK1. However, the substrates so formed are much poorer than those containing phosphate groups (5).
The following reagents are supplied with this product:
Store at (°C) Concentration NEBuffer™ for Protein Kinases (PK) -20 10 X
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